Wearedevelopingnewalgorithmsfordeterminationofprotein structures via NMR spectroscopy. By using the protein folding algorithms developed in the Friesner laboratory, we expect to be able to determine low resolution structures (3-5A RMS)with a small number of distance constraints, which will be easily obtained from an initial set of NMR data. This low resolution structure will then allow new experiments to be designed efficiently so as to quickly resolve the remaining NOE peaks, thus substantially reducing the time necessary to produce a high resolution structure. Results thus far are quite encouraging, using simulated data sets for myoglobin, 1-CTF, and lysozyme.